The major goals of this project are to determine if each of the three major proteins obtained during purification of exo-Beta-D-galactofuranosidase, contain enzyme activity and to determine if each has the same stability at an elevated temperature and at pH's ranging from 3.5 to 7. In addition, we hope to isolate and purify a carbohydrate-containing substance to i) determine if it protects against proteolytic inactivation of galactofuranosidase when added to galactofuranosidase preparations that have been freed of this substance, and ii) determine the composition and initiate the structural investigations of the carbohydrate-containing substance. We have previously shown that galactofuranosidase binds tightly to an affinity column containing peptidophosphogalactomannan as the ligand. The catalytically active site and the site at which the carbohydrate-containing substance binds appear not to be the same. Thus, we are attempting to determine the role of the carbohydrate-containing substance. BIBLIOGRAPHIC REFERENCES: Rietschel-Berst, M., Jentoft, N.H., Rick, P.D. & Gander, J.E. J. Biol. Chem. Extracellular Exo-Beta-Galactofuranosidase from Penicillium charlesii. Isolation, Purification and Properties. (in press). Gander, J.E. "Mono- and Oligosaccharides", Chapt. 14 in Plant Biochemistry, 3rd ed (Bonner, J. and Varner, J.E., eds.). (in press).